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Vol. 14, Issue 11, 4437-4447, November 2003
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* Department of Biochemistry, Weill Medical College of Cornell University, New York, New York 10021;
Department of Cell Biology, Washington University School of Medicine, St. Louis, Missouri 63110
Submitted April 15, 2003;
Revised June 3, 2003;
Accepted June 27, 2003
Monitoring Editor: Randy Schekman
The accurate assignment of molecular roles in membrane traffic is frequently complicated by the lack of specific inhibitors that can work on rapid time scales. Such inhibition schemes would potentially avoid the complications arising from either compensatory gene expression or the complex downstream consequences of inhibition of an important protein over long periods (>12 h). Here, we developed a novel chemical tool to disrupt clathrin function in living cells. We engineered a cross-linkable form of clathrin by using an FK506-binding protein 12 (FKBP)-clathrin fusion protein that is specifically oligomerized upon addition of the cell-permeant cross-linker FK1012-A. This approach interrupts the normal assembly-disassembly cycle of clathrin lattices and results in a specific, rapid, and reversible 
70% inhibition of clathrin function. This approach should be applicable to a number of proteins that must go through an assembly-disassembly cycle for normal function.
Corresponding author. E-mail address: taryan{at}med.cornell.edu. This article has been cited by other articles:
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